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Details on Person The C-propeptides are essential for the association of three...

Class:IdSummation:2002435
_displayNameThe C-propeptides are essential for the association of three...
_timestamp2012-05-24 15:44:18
created[InstanceEdit:2002388] Jupe, S, 2011-11-21
literatureReference[LiteratureReference:2002387] The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper
[LiteratureReference:2008082] The crucial role of trimerization domains in collagen folding
[LiteratureReference:2008075] The role of cis-trans isomerization of peptide bonds in the coil leads to and comes from triple helix conversion of collagen
[LiteratureReference:2008100] Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix leads to and comes from coil transition
modified[InstanceEdit:2008095] Jupe, S, 2011-11-21
[InstanceEdit:2267323] Jupe, S, 2012-05-24
textThe C-propeptides are essential for the association of three alpha chains into a trimeric non-helical procollagen. Alignment determines the composition of the trimer, brings the individual chains into the correct register and initiates formation of the triple helix at the C-terminus, which then proceeds to the N-terminus in a zipper-like fashion (Engel & Prockop 1991). Most early refolding studies were performed with collagen type III which contains a disulfide linkage at the C-terminus of its triple helix (Bächinger et al. 1978, Bruckner et al. 1978) that acts as a permanent linker even after removal of the non-collagenous domains.

Mutations within the C-propeptides further suggest that they are crucial for the correct interaction of the three polypeptide chains and for subsequent correct folding (refs. in Boudko et al. 2011).
(summation)[Reaction:2002401] Association of procollagen type XVIII [Homo sapiens]
[Reaction:8944214] Association of procollagen type I [Homo sapiens]
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No pathways have been reviewed or authored by The C-propeptides are essential for the association of three... (2002435)